Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9882342 | Archives of Biochemistry and Biophysics | 2005 | 6 Pages |
Abstract
The interaction of GroEL with non-native soluble proteins has been studied intensively and structure-function relationships have been established in considerable detail. Recently, we found that GroEL is also able to bind membrane proteins in the absence of detergents and deliver them to liposomes in a biologically active state. Here, we report that three well-studied membrane proteins (bacteriorhodopsin, LacY, and the bacteriophage λ holin) bind asymmetrically to tetradecameric GroEL. Each of the membrane proteins was visualized in one of the center cavities of GroEL using single particle analysis.
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Authors
Jingchuan Sun, Christos G. Savva, John Deaton, H. Ronald Kaback, Maja Svrakic, Ry Young, Andreas Holzenburg,